Abstract
The effects of 3-aminobenzamide (3ABm) and benzamide (BAm), known specific inhibitors of poly(ADP-ribose) polymerase (PARP), on actinomycin D (Act D)-induced apoptosis in HL-60 cells were examined. These inhibitors had no appreciable effect on apoptotic DNA fragmentation, chromatin condensation or PARP restriction cleavage, but clearly inhibited morphological changes, especially nuclear fragmentation and apoptotic-body formation, in a dose-dependent manner. These results suggest that the synthesis of ADP-ribose polymers is not essential for the progression of apoptotic DNA fragmentation and chromatin condensation, but is required in the processes leading to nuclear fragmentation and the subsequent apoptotic-body formation during apoptosis in HL-60 cells.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aminobenzoates / pharmacology
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Apoptosis / drug effects*
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Benzamides / pharmacology
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Benzoates / pharmacology
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Benzoic Acid
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Blotting, Western
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Cell Nucleus / drug effects
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Cell Nucleus / physiology*
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DNA Fragmentation / drug effects*
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Dactinomycin / pharmacology
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Dose-Response Relationship, Drug
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Enzyme Inhibitors / pharmacology
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HL-60 Cells
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Humans
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Microscopy, Electron
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Microscopy, Fluorescence
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Poly(ADP-ribose) Polymerase Inhibitors
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Poly(ADP-ribose) Polymerases / analysis
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Poly(ADP-ribose) Polymerases / physiology*
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meta-Aminobenzoates
Substances
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Aminobenzoates
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Benzamides
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Benzoates
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Enzyme Inhibitors
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Poly(ADP-ribose) Polymerase Inhibitors
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meta-Aminobenzoates
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Dactinomycin
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benzamide
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3-aminobenzamide
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Benzoic Acid
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Poly(ADP-ribose) Polymerases
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3-aminobenzoic acid